Biology: The Dynamic Science (MindTap Course List)
4th Edition
ISBN: 9781305389892
Author: Peter J. Russell, Paul E. Hertz, Beverly McMillan
Publisher: Cengage Learning
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Chapter 9, Problem 11TYK
Discuss Concepts Describe the possible ways in which a G-protein–coupled receptor pathway could become defective and not trigger any cellular responses.
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Students have asked these similar questions
GTP is an important high-energy molecule that facilitates the activation of many cellular sig-
nal transduction pathways. Certain genetic dysfunctions can inhibit the ability of a cell to
synthesize GTP.
Which of the following describes the most direct result of GTP synthesis inhibition?
A
B
с
D
The cell would be able to carry out reception and transduction but would not be able to
produce the cellular response in the relevant signal transduction pathway.
The G protein-coupled receptor will not be able to bind corresponding ligands, inhibiting
the reception components of the relevant signal transduction pathway.
The cell will use ATP instead of GTP to activate the G protein on the intracellular region
of the G protein-coupled receptor.
The cell would not be able to activate G proteins on the intracellular regions of G pro-
tein-coupled receptors.
Draw the general structural features of a G-protein coupled receptor (GPCR)
. which of the following statements about heterotrimetric G proteins and their receptors is incorrect?
A: when GTP binds to the alpha subunit of the G protein, the beta-gamma subunit dissociates from the alpha subunit
B: G-protein coupled receptors contain nine transmembrane alpha helices
C: binding of arrestin causes removal of the receptor from the membrane
D: G protein- coupled receptors may be desensitized by serine phosphorylation
I had chosen option A and got it wrong. What is the Correct answer and explain how it is. Also, where did i go wrong in choosing option A?
Chapter 9 Solutions
Biology: The Dynamic Science (MindTap Course List)
Ch. 9.1 - What accounts for the specificity of a cellular...Ch. 9.2 - Prob. 1SBCh. 9.2 - Prob. 2SBCh. 9.3 - Prob. 1SBCh. 9.3 - Prob. 2SBCh. 9.3 - Prob. 3SBCh. 9.3 - Prob. 4SBCh. 9.3 - Prob. 5SBCh. 9.3 - Prob. 6SBCh. 9.4 - What distinguishes a steroid receptor from a...
Ch. 9.4 - By what means does a specific steroid hormone...Ch. 9.5 - Prob. 1SBCh. 9 - In signal transduction, which of the following is...Ch. 9 - Which of the following could not elicit a signal...Ch. 9 - A cell that responds to a signaling molecule is...Ch. 9 - Prob. 4TYKCh. 9 - Prob. 5TYKCh. 9 - Which of the following is incorrect about pathways...Ch. 9 - Which of the following would not inhibit signal...Ch. 9 - Prob. 8TYKCh. 9 - Prob. 9TYKCh. 9 - Prob. 10TYKCh. 9 - Discuss Concepts Describe the possible ways in...Ch. 9 - Discuss Concepts Is providing extra insulin an...Ch. 9 - Discuss Concepts There are molecules called GTP...Ch. 9 - Discuss Concepts Why do you suppose cells evolved...Ch. 9 - How would you set up an experiment to determine...Ch. 9 - Prob. 16TYKCh. 9 - Prob. 1ITDCh. 9 - Prob. 2ITDCh. 9 - Prob. 3ITD
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- The G protein coupled receptor (GPCR) pathway elicits diverse intracellular responses in different cells. The basic steps of GPCR signaling are outlined in this diagram. Which of the following statements correctly describes the process of GPCR signaling? The GPCR activation is reversible after the signal of the ligand diminishes. The membrane-embedded enzyme uses GTP as a secondary messenger to initiate gene expression. The ligand attaches to both the GPCR and the membrane-embedded enzyme to activate the GPCR pathway. The ligand-bound GPCR sends a GTP molecule to an enzyme in the membrane and switches it into an active state.arrow_forwardContinuous exposure of a G protein-coupled receptor to its ligand leads to a phenomenon known as desensitization. Describe several molecule mechanisms for receptor desensitizationarrow_forwardIf you have a protein kinase that is regulated by both small molecule inhibitors as well as by phosphorylation, and is part of a cooperative enzyme complex that works as part of a larger pathway involving kinase and GTPase proteins please explain where on this protein regulation could occur, how different types of inhibition could control the function of the protein as well as the function of the complex, and how the protein could regulate other proteins. (This question was previously answered but it was answered incompletely mentioning an herbicide developed in the 1950's. Apparently, it was a plagiarized excerpt from an NCBI article. This is a repost for a full and complete answer. Thank you so much for your help! :) )arrow_forward
- Suppose that Protein J which is a hypothetical protein kinase receptor was determined to be related to the progression of cancer through its activation. It was also determined that the protein exists in the active and inactive forms. The said active form is highly similar to the Protein K's conformation. Ligands A, B, and C, which are lead inhibitor compounds, were optimized to inhibit Protein J. The affinities of the ligands are shown in the table. Kp values Active Protein J Inactive Protein J Protein K Ligand A 10 mM 20 nM 5 mM Ligand B 20 nM 10 mM 15 nM Ligand C 20 nM 15 nM 15 nM Question: a. Which of the ligands, based on the table, has the highest specificity in binding to the target Protein J?arrow_forwardSuppose that Protein J which is a hypothetical protein kinase receptor was determined to be related to the progression of cancer through its activation. It was also determined that the protein exists in the active and inactive forms. The said active form is highly similar to the Protein K's conformation. Ligands A, B, and C, which are lead inhibitor compounds, were optimized to inhibit Protein J. The affinities of the ligands are shown in the table. Kp values Active Protein J Inactive Protein J Protein K Ligand A 10 mM 20 nM 5 mM Ligand B 20 nM 10 mM 15 nM Ligand C 20 nM 15 nM 15 nM Question: a. Which of the ligands, based on the table, may be expected to be the most potent or have the highest activity against cancer? Explain. b. Which of the ligands, based on the table, may be expected to be least toxic to normal cells? Explain.arrow_forwardSuppose that Protein J which is a hypothetical protein kinase receptor was determined to be related to the progression of cancer through its activation. It was also determined that the protein exists in the active and inactive forms. The said active form is highly similar to the Protein K's conformation. Ligands A, B, and C, which are lead inhibitor compounds, were optimized to inhibit Protein J. The affinities of the ligands are shown in the table. Kp values Active Protein J Inactive Protein J Protein K Ligand A 10 mM 20 nM 5 mM Ligand B 20 nM 10 mM 15 nM Ligand C 20 nM 15 nM 15 nM Question: Describe the relative binding affinities of Ligand A to Protein K and to the active and inactive forms of Protein J. Determine which will Ligand A bind with the highest, medium, and lowest affinity.arrow_forward
- Describe the common architecture of G protein-coupled receptors. Illustrate your answer with reference to the domains that facilitate signal transduction across the plasma membranearrow_forwardGTP-binding proteins play critical roles in many signal transductions through G proteins. Describe two examples in which G proteins act and compare the role of the G proteins in each case.arrow_forwardLigand binding to proteins may occur with varying strengths; some ligands bind tightly to proteins while others bind less tightly. The strengths of reversible binding are determined experimentally by varying concentrations of ligands, and measuring the saturation of the protein in the various ligand concentrations. One such laboratory study investigated the binding of a hormone to three different receptor proteins in the cell membrane. The data collected are shown in the table below: 1) Provide a brief explanation as to why ligand binding to proteins must be a reversible process. 2) Calculate the dissociation constant (Kd) for the hormone binding to each of the three proteins.arrow_forward
- Ligand binding to proteins may occur with varying strengths; some ligands bind tightly to proteins while others bind less tightly. The strengths of reversible binding are determined experimentally by varying concentrations of ligands, and measuring the saturation of the protein in the various ligand concentrations. One such laboratory study investigated the binding of a hormone to three different receptor proteins in the cell membrane. The data collected are shown in the table below 1) Which of the proteins demonstrate the tightest/strongest binding of the hormone? Which demonstrates the least tight binding of the hormone? What is the basis for your answer?arrow_forwardUpon activation by a receptor, a G protein exchanges bound GDP for GTP, rather than phosphorylating GDP that is already bound. Similarly, the a subunit-GTP complex has a slow GTPase activity that hydrolyzes bound GTP, rather than exchanging it for GDP. Describe experimental evidence that would be consistent with these conclusions.arrow_forwardPane Create a diagram which illustrates the typical signalling mechanism of action of g protein coupled and possible routes of communication (autocrine etc.). Should show the specific molecules involved, the mechanisms of signal transduction and indicate the different pathways that are activated. It should include a specific example of a receptor, ligand and signalling pathway for each general class. Include as wide a variety of ligands and modes of action as you can. for a novel pathway. Superfamily Give the superfamily to which the receptor belongs Accession Give the Uniprot accession number Name Give the molecule name Species Give the species Ligand What is the ligand, or class of ligands which bind to this receptor? Key What are the physiological processes involved? Is this autocrine, physiological paracrine or endocrine or some combination of them? What is the pathology of the receptor? process involved What are the downstream actions of the receptor? Which molecules does it…arrow_forward
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